New insights into intra- and intermolecular interactions of immunoglobulins: crystal structure of mouse IgG2b-Fc at 2.1-A resolution

Immunology. 2009 Mar;126(3):378-85. doi: 10.1111/j.1365-2567.2008.02904.x. Epub 2008 Sep 6.

Abstract

The structure of the Fc fragment of monoclonal antibody IgG2b from hybridom M75 of Mus musculus has been determined by single crystal X-ray diffraction. This is the first report of the structure of the murine immunoglobulin isotype IgG2b. The structure refined at 2.1 A resolution provides more detailed structural information about native oligosaccharides than was previously available. High-quality Fourier maps provide a clear identification of alpha-l-fucose with partial occupancy in the first branch of the antennary oligosaccharides. A unique Fc:Fc interaction was observed at the C(H)2-C(H)3 interface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / chemistry
  • Antigen-Antibody Complex / chemistry
  • Crystallization
  • Crystallography, X-Ray / methods
  • Glycosylation
  • Immunoglobulin Fc Fragments / chemistry*
  • Immunoglobulin G / chemistry*
  • Mice
  • Oligosaccharides / chemistry
  • Protein Structure, Secondary

Substances

  • Antibodies, Monoclonal
  • Antigen-Antibody Complex
  • Immunoglobulin Fc Fragments
  • Immunoglobulin G
  • Oligosaccharides